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17β-Hydroxysteroid dehydrogenase

class of enzymes

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Record originEnglish Wikipedia
Text licenseCC BY-SA 4.0
Source revisionMar 9, 2026
Entity authorityQ86201640
Source-derived summary

17β-Hydroxysteroid dehydrogenases (17β-HSD, HSD17B) (EC 1.1.1.51), also 17-ketosteroid reductases (17-KSR), are a group of alcohol oxidoreductases which catalyze the reduction of 17-ketosteroids and the dehydrogenation of 17β-hydroxysteroids in steroidogenesis and steroid metabolism. This includes interconversion of DHEA and androstenediol, androstenedione and testosterone, and estrone and estradiol.

The major reactions catalyzed by 17β-HSD (such as the conversion of androstenedione to testosterone) are hydrogenation (reduction) reactions, rather than dehydrogenation (oxidation) reactions.

Reactions

17β-HSDs catalyze the following redox reactions of sex steroids:

20α-Hydroxyprogesterone ↔ Progesterone

DHEATooltip Dehydroepiandrosterone ↔ Androstenediol

Androstenedione ↔ Testosterone

Dihydrotestosterone ↔ 5α-Androstanedione / 3α-Androstanediol / 3β-Androstanediol

Estrone ↔ Estradiol

16α-Hydroxyestrone ↔ Estriol

Activity distribution

Genes

Genes coding for 17β-HSD include:

HSD17B1: Referred to as "estrogenic". Major subtype for activation of estrogens from weaker forms (estrone to estradiol and 16α-hydroxyestrone to estriol). Catalyzes the final step in the biosynthesis of estrogens. Highly selective for estrogens; 100-fold higher affinity for estranes over androstanes. However, also catalyzes the conversion of DHEA into androstenediol. Recently, has been found to inactivate DHT into 3α- and 3β-androstanediol. Expressed primarily in the ovaries and placenta but also at lower levels in the breast epithelium.

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The public source identifies “17β-Hydroxysteroid dehydrogenase” as class of enzymes. This brief keeps that definition visible, then builds a research path around 17β-Hydroxysteroid, dehydrogenase and class.

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This entry incorporates text from 17β-Hydroxysteroid dehydrogenase” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.